HEADER APOPTOSIS 27-DEC-06 2JCN
TITLE THE CRYSTAL STRUCTURE OF BAK1 - A MITOCHONDRIAL APOPTOSIS
TITLE 2 REGULATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: APOPTOSIS REGULATOR BAK, BCL-2-LIKE 7 PROTEIN, BAK1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: RESIDUE 23-184 GAP AT 50-54
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS APOPTOSIS, MITOCHONDRIAL OUTER MEMBRANE PERMEABILIZATION,
KEYWDS 2 OLIGOMERIZATION, CYTOCHROME C RELEASE, MEMBRANE, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MOCHE,P.STENMARK,C.ARROWSMITH,H.BERGLUND,R.BUSAM,R.COLLINS,
AUTHOR 2 A.EDWARDS,U.B.ERICSSON,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,
AUTHOR 3 B.M.HALLBERG,L.HOLMBERG SCHIAVONE,I.JOHANSSON,T.KARLBERG,U.KOSINSKA,
AUTHOR 4 T.KOTENYOVA,S.LUNDGREN,M.E.NILSSON,T.NYMAN,D.OGG,C.PERSSON,
AUTHOR 5 J.SAGEMARK,M.SUNDSTROM,J.UPPENBERG,M.UPSTEN,A.G.THORSELL,
AUTHOR 6 S.VAN DEN BERG,J.WEIGELT,P.NORDLUND,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 7 (SGC)
REVDAT 4 13-JUL-11 2JCN 1 VERSN
REVDAT 3 24-FEB-09 2JCN 1 VERSN
REVDAT 2 08-MAY-07 2JCN 1 AUTHOR REMARK
REVDAT 1 04-JAN-07 2JCN 0
JRNL AUTH M.MOCHE,P.STENMARK,C.ARROWSMITH,H.BERGLUND,R.BUSAM,
JRNL AUTH 2 R.COLLINS,A.EDWARDS,U.B.ERICSSON,S.FLODIN,A.FLORES,
JRNL AUTH 3 S.GRASLUND,M.HAMMARSTROM,B.M.HALLBERG,L.HOLMBERG SCHIAVONE,
JRNL AUTH 4 I.JOHANSSON,T.KARLBERG,U.KOSINSKA,T.KOTENYOVA,S.LUNDGREN,
JRNL AUTH 5 M.E.NILSSON,T.NYMAN,D.OGG,C.PERSSON,J.SAGEMARK,M.SUNDSTROM,
JRNL AUTH 6 J.UPPENBERG,M.UPSTEN,A.G.THORSELL,S.VAN DEN BERG,J.WEIGELT,
JRNL AUTH 7 P.NORDLUND
JRNL TITL THE CRYSTAL STRUCTURE OF BAK1 - AN APOPTOSIS TRIGGER IN THE
JRNL TITL 2 MITOCHONDRIAL OUTER MEMBRANE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 14832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 785
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1064
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1830
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1281
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -0.42000
REMARK 3 B12 (A**2) : 0.14000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.156
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1318 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1164 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1789 ; 1.426 ; 1.924
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2687 ; 0.915 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 159 ; 7.420 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 72 ;33.478 ;23.472
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 209 ;15.563 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;12.117 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 189 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1494 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 298 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 296 ; 0.236 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1154 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 671 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 717 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 56 ; 0.188 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 22 ; 0.342 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 75 ; 0.248 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.202 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1018 ; 1.579 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1257 ; 1.858 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 629 ; 2.554 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 531 ; 3.412 ; 5.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 43
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5270 27.3830 -5.1220
REMARK 3 T TENSOR
REMARK 3 T11: -0.0056 T22: 0.1187
REMARK 3 T33: 0.0484 T12: 0.0100
REMARK 3 T13: -0.0038 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 2.5560 L22: 10.9955
REMARK 3 L33: 4.1806 L12: 1.4965
REMARK 3 L13: 0.2024 L23: -1.3135
REMARK 3 S TENSOR
REMARK 3 S11: -0.1009 S12: 0.1839 S13: 0.0640
REMARK 3 S21: 0.1673 S22: 0.2852 S23: -0.2058
REMARK 3 S31: 0.1307 S32: 0.0489 S33: -0.1843
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 44 A 67
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3580 39.5800 -10.4990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0743 T22: 0.1497
REMARK 3 T33: 0.1440 T12: -0.1027
REMARK 3 T13: -0.0339 T23: 0.1302
REMARK 3 L TENSOR
REMARK 3 L11: 7.6206 L22: 10.7749
REMARK 3 L33: 2.9892 L12: 7.1317
REMARK 3 L13: -2.7905 L23: -2.9763
REMARK 3 S TENSOR
REMARK 3 S11: -0.7559 S12: 0.9991 S13: 0.7434
REMARK 3 S21: -1.1564 S22: 0.9258 S23: 0.8575
REMARK 3 S31: 0.0115 S32: -0.4129 S33: -0.1699
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 68 A 83
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7070 30.1760 -10.1100
REMARK 3 T TENSOR
REMARK 3 T11: -0.0146 T22: 0.1786
REMARK 3 T33: 0.0685 T12: 0.0203
REMARK 3 T13: -0.0413 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 6.2799 L22: 21.2239
REMARK 3 L33: 8.3641 L12: -7.2561
REMARK 3 L13: -3.8236 L23: 6.0718
REMARK 3 S TENSOR
REMARK 3 S11: 0.1930 S12: 0.2660 S13: 0.2127
REMARK 3 S21: -0.3532 S22: -0.3107 S23: 0.5335
REMARK 3 S31: -0.4685 S32: -0.9315 S33: 0.1177
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 84 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9570 42.5030 7.2860
REMARK 3 T TENSOR
REMARK 3 T11: -0.0045 T22: 0.0284
REMARK 3 T33: 0.0949 T12: 0.0365
REMARK 3 T13: 0.1252 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 19.1112 L22: 5.1500
REMARK 3 L33: 10.2383 L12: 0.3246
REMARK 3 L13: 4.1716 L23: 2.3336
REMARK 3 S TENSOR
REMARK 3 S11: 0.3894 S12: 0.0287 S13: 0.9808
REMARK 3 S21: -0.0690 S22: -0.3036 S23: 0.5214
REMARK 3 S31: -0.7939 S32: -0.9192 S33: -0.0858
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 104 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5140 33.8290 5.8260
REMARK 3 T TENSOR
REMARK 3 T11: -0.0217 T22: 0.0758
REMARK 3 T33: 0.0678 T12: -0.0138
REMARK 3 T13: 0.0302 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 4.0110 L22: 1.9382
REMARK 3 L33: 3.4258 L12: 1.6568
REMARK 3 L13: -1.0928 L23: -0.7364
REMARK 3 S TENSOR
REMARK 3 S11: 0.2376 S12: -0.3369 S13: 0.2432
REMARK 3 S21: 0.1065 S22: -0.0992 S23: 0.0836
REMARK 3 S31: -0.1577 S32: 0.1368 S33: -0.1383
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 162 A 184
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7800 20.7470 0.7030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0323 T22: 0.0771
REMARK 3 T33: 0.0715 T12: -0.0439
REMARK 3 T13: -0.0033 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 3.3233 L22: 2.1752
REMARK 3 L33: 8.1485 L12: 0.0692
REMARK 3 L13: 0.6798 L23: -1.5338
REMARK 3 S TENSOR
REMARK 3 S11: -0.1462 S12: 0.1692 S13: -0.0508
REMARK 3 S21: -0.0717 S22: 0.0338 S23: 0.0473
REMARK 3 S31: 0.2264 S32: -0.1826 S33: 0.1124
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. THERE IS A CYSTEINE S-S BRIDGE BETWEEN
REMARK 3 CYS166 AND CYS166 FROM A SYMMETRY MOLECULE
REMARK 4
REMARK 4 2JCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JAN-07.
REMARK 100 THE PDBE ID CODE IS EBI-30940.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 313450
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 20.170
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 20.70
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: OTHER
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 20% GLYCEROL, 0.2M
REMARK 280 SODIUM SULPHATE, 2MM TCEP, 0.3M NACL, 20 MM HEPES PH7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.04667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.02333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.03500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 23.01167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 115.05833
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 92.04667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 46.02333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 23.01167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 69.03500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 115.05833
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH A2011 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 19
REMARK 465 MET A 20
REMARK 465 SER A 21
REMARK 465 ALA A 22
REMARK 465 GLU A 50
REMARK 465 GLY A 51
REMARK 465 VAL A 52
REMARK 465 ALA A 53
REMARK 465 ALA A 54
REMARK 465 ASN A 185
REMARK 465 GLY A 186
REMARK 465 PRO A 187
REMARK 465 ILE A 188
REMARK 465 LEU A 189
REMARK 465 ASN A 190
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 121 O HOH A 2051 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 57 94.69 -160.88
REMARK 500 LEU A 65 33.98 -146.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 64 LEU A 65 -117.80
REMARK 500 GLY A 122 ILE A 123 146.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BXL RELATED DB: PDB
REMARK 900 STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX,
REMARK 900 NMR, MINIMIZED AVERAGE STRUCTURE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 COMPARED TO OUR CLONED AND TEV CLEAVED CONSTRUCT WE MISS 4AA
REMARK 999 IN THE N-TERMINUS AND 6AA IN THE C-TERMINUS. IN ADDITION
REMARK 999 WE HAVE A GAP BETWEEN RESIDUE 50-54 IN THIS STRUCTURE.
DBREF 2JCN A 19 20 PDB 2JCN 2JCN 19 20
DBREF 2JCN A 21 190 UNP Q16611 BAK_HUMAN 21 190
SEQRES 1 A 172 SER MET SER ALA SER GLU GLU GLN VAL ALA GLN ASP THR
SEQRES 2 A 172 GLU GLU VAL PHE ARG SER TYR VAL PHE TYR ARG HIS GLN
SEQRES 3 A 172 GLN GLU GLN GLU ALA GLU GLY VAL ALA ALA PRO ALA ASP
SEQRES 4 A 172 PRO GLU MET VAL THR LEU PRO LEU GLN PRO SER SER THR
SEQRES 5 A 172 MET GLY GLN VAL GLY ARG GLN LEU ALA ILE ILE GLY ASP
SEQRES 6 A 172 ASP ILE ASN ARG ARG TYR ASP SER GLU PHE GLN THR MET
SEQRES 7 A 172 LEU GLN HIS LEU GLN PRO THR ALA GLU ASN ALA TYR GLU
SEQRES 8 A 172 TYR PHE THR LYS ILE ALA THR SER LEU PHE GLU SER GLY
SEQRES 9 A 172 ILE ASN TRP GLY ARG VAL VAL ALA LEU LEU GLY PHE GLY
SEQRES 10 A 172 TYR ARG LEU ALA LEU HIS VAL TYR GLN HIS GLY LEU THR
SEQRES 11 A 172 GLY PHE LEU GLY GLN VAL THR ARG PHE VAL VAL ASP PHE
SEQRES 12 A 172 MET LEU HIS HIS CYS ILE ALA ARG TRP ILE ALA GLN ARG
SEQRES 13 A 172 GLY GLY TRP VAL ALA ALA LEU ASN LEU GLY ASN GLY PRO
SEQRES 14 A 172 ILE LEU ASN
HET SO4 A1001 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *89(H2 O)
HELIX 1 1 SER A 23 GLU A 48 1 26
HELIX 2 2 ASP A 57 VAL A 61 5 5
HELIX 3 3 SER A 69 GLY A 82 1 14
HELIX 4 4 ASP A 84 GLN A 101 1 18
HELIX 5 5 ASN A 106 PHE A 119 1 14
HELIX 6 6 ASN A 124 HIS A 145 1 22
HELIX 7 7 PHE A 150 HIS A 165 1 16
HELIX 8 8 CYS A 166 ARG A 174 1 9
HELIX 9 9 GLY A 176 LEU A 183 5 8
SITE 1 AC1 9 ASN A 124 TRP A 125 GLY A 152 ARG A 156
SITE 2 AC1 9 TRP A 170 ARG A 174 HOH A2054 HOH A2067
SITE 3 AC1 9 HOH A2089
CRYST1 62.770 62.770 138.070 90.00 90.00 120.00 P 65 2 2 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015931 0.009198 0.000000 0.00000
SCALE2 0.000000 0.018396 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007243 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
